|
Name |
Accession |
Description |
Interval |
E-value |
| groEL |
PRK00013 |
chaperonin GroEL; Reviewed |
2-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 234573 Cd Length: 542 Bit Score: 995.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 2 AAKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
Cdd:PRK00013 1 MAKDIKFGEDARRKLLRGVNKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 82 NDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGLD 161
Cdd:PRK00013 81 NDVAGDGTTTATVLAQAIVREGLKNVAAGANPMDLKRGIDKAVEAAVEELKKISKPVEDKEEIAQVATISANGDEEIGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 162 IAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAVV 241
Cdd:PRK00013 161 IAEAMEKVGKEGVITVEESKGFETELEVVEGMQFDRGYLSPYFVTDPEKMEAELENPYILITDKKISNIQDLLPVLEQVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 242 QTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRAK 321
Cdd:PRK00013 241 QSGKPLLIIAEDVEGEALATLVVNKLRGTLKVVAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDATLEDLGQAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 322 KVSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDALN 401
Cdd:PRK00013 321 KVVVTKDNTTIVDGAGDKEAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 402 ATRAAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNA 480
Cdd:PRK00013 401 ATRAAVEEGIVPGGGVALLRAAPALeALKGLNGDEATGINIVLRALEAPLRQIAENAGLEGSVVVEKVKNGKGKGYGYNA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 499269991 481 QTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 531
Cdd:PRK00013 481 ATGEYVDMIEAGIIDPTKVTRSALQNAASVAGLLLTTEAVVADKPEKKAAA 531
|
|
| groEL |
PRK12849 |
chaperonin GroEL; Reviewed |
2-530 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237230 Cd Length: 542 Bit Score: 942.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 2 AAKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
Cdd:PRK12849 1 MAKIIKFDEEARRALERGVNKLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPFENLGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 82 NDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGLD 161
Cdd:PRK12849 81 NDVAGDGTTTATVLAQALVQEGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVSGSEEIAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 162 IAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAVV 241
Cdd:PRK12849 161 IAEAMEKVGKDGVITVEESKTLETELEVTEGMQFDRGYLSPYFVTDPERMEAVLEDPLILLTDKKISSLQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 242 QTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRAK 321
Cdd:PRK12849 241 QSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGLKLEEVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 322 KVSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDALN 401
Cdd:PRK12849 321 RVTITKDNTTIVDGAGDKEAIEARVAQIRRQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATEVELKERKDRVEDALN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 402 ATRAAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNtDDFGYNA 480
Cdd:PRK12849 401 ATRAAVEEGIVPGGGVALLRAAKALDeLAGLNGDQAAGVEIVRRALEAPLRQIAENAGLDGSVVVAKVLELE-DGFGFNA 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 499269991 481 QTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAP 530
Cdd:PRK12849 480 ATGEYGDLIAAGIIDPVKVTRSALQNAASVAGLLLTTEALVADKPEEEDP 529
|
|
| groEL |
PRK12850 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237231 Cd Length: 544 Bit Score: 931.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 1 MAAKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
Cdd:PRK12850 1 MAAKEIRFSTDARDRLLRGVNILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVKEVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 81 TNDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGL 160
Cdd:PRK12850 81 TNDLAGDGTTTATVLAQAIVREGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 161 DIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAV 240
Cdd:PRK12850 161 MIAEAMDKVGKEGVITVEEAKTLGTELDVVEGMQFDRGYLSPYFVTNPEKMRAELEDPYILLHEKKISNLQDLLPILEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 241 VQTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRA 320
Cdd:PRK12850 241 VQSGRPLLIIAEDVEGEALATLVVNKLRGGLKSVAVKAPGFGDRRKAMLEDIAVLTGGQVISEDLGIKLENVTLDMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 321 KKVSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDAL 400
Cdd:PRK12850 321 KRVLITKENTTIIDGAGDKKNIEARVKQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 401 NATRAAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEkNTDDFGYN 479
Cdd:PRK12850 401 HATRAAVEEGIVPGGGVALLRARSALRgLKGANADETAGIDIVRRALEEPLRQIATNAGFEGSVVVGKVAE-LPGNFGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499269991 480 AQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 531
Cdd:PRK12850 480 AQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAAAA 531
|
|
| GroEL |
cd03344 |
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ... |
4-523 |
0e+00 |
|
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239460 Cd Length: 520 Bit Score: 911.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 4 KEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTND 83
Cdd:cd03344 1 KDIKFGEEARKALLRGVNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPFENMGAQLVKEVASKTND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 84 IAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGLDIA 163
Cdd:cd03344 81 VAGDGTTTATVLARAIIKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKPVKTKEEIAQVATISANGDEEIGELIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 164 EAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAVVQT 243
Cdd:cd03344 161 EAMEKVGKDGVITVEEGKTLETELEVVEGMQFDRGYLSPYFVTDPEKMEVELENPYILLTDKKISSIQELLPILELVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 244 GKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRAKKV 323
Cdd:cd03344 241 GRPLLIIAEDVEGEALATLVVNKLRGGLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEELGLKLEDVTLEDLGRAKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 324 SITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDALNAT 403
Cdd:cd03344 321 VVTKDDTTIIGGAGDKAAIKARIAQIRKQIEETTSDYDKEKLQERLAKLSGGVAVIKVGGATEVELKEKKDRVEDALNAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 404 RAAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNtDDFGYNAQT 482
Cdd:cd03344 401 RAAVEEGIVPGGGVALLRASPALdKLKALNGDEKLGIEIVRRALEAPLRQIAENAGVDGSVVVEKVLESP-DGFGYDAAT 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 499269991 483 GEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAE 523
Cdd:cd03344 480 GEYVDMIEAGIIDPTKVVRSALQNAASVASLLLTTEALVVD 520
|
|
| groEL |
PRK12852 |
chaperonin GroEL; Reviewed |
1-530 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 237232 Cd Length: 545 Bit Score: 906.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 1 MAAKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
Cdd:PRK12852 1 MAAKDVKFSGDARDRMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 81 TNDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGL 160
Cdd:PRK12852 81 TNDLAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 161 DIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAV 240
Cdd:PRK12852 161 MIAQAMQKVGNEGVITVEENKSLETEVDIVEGMKFDRGYLSPYFVTNAEKMTVELDDAYILLHEKKLSGLQAMLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 241 VQTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRA 320
Cdd:PRK12852 241 VQSGKPLLIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQLISEDLGIKLENVTLKMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 321 KKVSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDAL 400
Cdd:PRK12852 321 KKVVIDKENTTIVNGAGKKADIEARVGQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVEDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 401 NATRAAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYN 479
Cdd:PRK12852 401 NATRAAVQEGIVPGGGVALLRAKKAVGrINNDNADVQAGINIVLKALEAPIRQIAENAGVEGSIVVGKILENKSETFGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 499269991 480 AQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAP 530
Cdd:PRK12852 481 AQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKKDAA 531
|
|
| GroEL |
TIGR02348 |
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES ... |
3-526 |
0e+00 |
|
chaperonin GroL; This family consists of GroEL, the larger subunit of the GroEL/GroES cytosolic chaperonin. It is found in bacteria, organelles derived from bacteria, and occasionally in the Archaea. The bacterial GroEL/GroES group I chaperonin is replaced a group II chaperonin, usually called the thermosome in the Archaeota and CCT (chaperone-containing TCP) in the Eukaryota. GroEL, thermosome subunits, and CCT subunits all fall under the scope of pfam00118. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274089 Cd Length: 524 Bit Score: 861.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 3 AKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTN 82
Cdd:TIGR02348 1 AKQIKFDEEARKALLRGVDKLADAVKVTLGPKGRNVVLEKSFGAPTITKDGVTVAKEIELEDKFENMGAQLVKEVASKTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 83 DIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGLDI 162
Cdd:TIGR02348 81 DVAGDGTTTATVLAQAIVKEGLKNVAAGANPIELKRGIEKAVEAVVEELKKLSKPVKGKKEIAQVATISANNDEEIGSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 163 AEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAVVQ 242
Cdd:TIGR02348 161 AEAMEKVGKDGVITVEESKSLETELEVVEGMQFDRGYISPYFVTDAEKMEVELENPYILITDKKISNIKDLLPLLEKVAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 243 TGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRAKK 322
Cdd:TIGR02348 241 SGKPLLIIAEDVEGEALATLVVNKLRGTLNVCAVKAPGFGDRRKAMLEDIAILTGGQVISEELGLKLEEVTLDDLGKAKK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 323 VSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDALNA 402
Cdd:TIGR02348 321 VTVDKDNTTIVEGAGDKAAIKARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIKVGAATETEMKEKKLRIEDALNA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 403 TRAAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNtDDFGYNAQ 481
Cdd:TIGR02348 401 TRAAVEEGIVPGGGVALLRAAAALeGLKGDGEDEAIGIDIVKRALEAPLRQIAENAGLDGAVVAEKVKELK-GNFGFNAA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 499269991 482 TGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPK 526
Cdd:TIGR02348 480 TGEYEDLVEAGIIDPTKVTRSALQNAASIAGLLLTTEAVVADKPE 524
|
|
| groEL |
PRK12851 |
chaperonin GroEL; Reviewed |
1-531 |
0e+00 |
|
chaperonin GroEL; Reviewed
Pssm-ID: 171770 Cd Length: 541 Bit Score: 850.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 1 MAAKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
Cdd:PRK12851 1 MAAKEVKFHVEAREKMLRGVNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 81 TNDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGL 160
Cdd:PRK12851 81 TNDVAGDGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATISANGDAEIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 161 DIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAV 240
Cdd:PRK12851 161 LVAEAMEKVGNEGVITVEESKTAETELEVVEGMQFDRGYLSPYFVTDADKMEAELEDPYILIHEKKISNLQDLLPVLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 241 VQTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRA 320
Cdd:PRK12851 241 VQSGKPLLIIAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLENVTLEQLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 321 KKVSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDAL 400
Cdd:PRK12851 321 KKVVVEKENTTIIDGAGSKTEIEGRVAQIRAQIEETTSDYDREKLQERLAKLAGGVAVIRVGASTEVEVKEKKDRVDDAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 401 NATRAAVQEGIVPGGGVALLRSSVKI-TVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKnTDDFGYN 479
Cdd:PRK12851 401 HATRAAVEEGIVPGGGVALLRAVKALdKLETANGDQRTGVEIVRRALEAPVRQIAENAGAEGSVVVGKLREK-PGGYGFN 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499269991 480 AQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 531
Cdd:PRK12851 480 AATNEYGDLYAQGVIDPVKVVRTALQNAASVAGLLLTTEAMVAEKPKKEPAP 531
|
|
| PTZ00114 |
PTZ00114 |
Heat shock protein 60; Provisional |
2-530 |
0e+00 |
|
Heat shock protein 60; Provisional
Pssm-ID: 185455 Cd Length: 555 Bit Score: 789.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 2 AAKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
Cdd:PTZ00114 13 KGKEIRFGDEARQSLLKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFENVGAQLIRQVASKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 82 NDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGLD 161
Cdd:PTZ00114 93 NDKAGDGTTTATILARAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRPVKTKEDILNVATISANGDVEIGSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 162 IAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAVV 241
Cdd:PTZ00114 173 IADAMDKVGKDGTITVEDGKTLEDELEVVEGMSFDRGYISPYFVTNEKTQKVELENPLILVTDKKISSIQSILPILEHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 242 QTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISED-LGIKLESVTLDMLGRA 320
Cdd:PTZ00114 253 KNKRPLLIIAEDVEGEALQTLIINKLRGGLKVCAVKAPGFGDNRKDILQDIAVLTGATVVSEDnVGLKLDDFDPSMLGSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 321 KKVSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDAL 400
Cdd:PTZ00114 333 KKVTVTKDETVILTGGGDKAEIKERVELLRSQIERTTSEYDKEKLKERLAKLSGGVAVIKVGGASEVEVNEKKDRIEDAL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 401 NATRAAVQEGIVPGGGVALLRSSVKI-TVKGEND---DQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDF 476
Cdd:PTZ00114 413 NATRAAVEEGIVPGGGVALLRASKLLdKLEEDNEltpDQRTGVKIVRNALRLPTKQIAENAGVEGAVVVEKILEKKDPSF 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 499269991 477 GYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAP 530
Cdd:PTZ00114 493 GYDAQTGEYVNMFEAGIIDPTKVVRSALVDAASVASLMLTTEAAIVDLPKEKKK 546
|
|
| PRK14104 |
PRK14104 |
chaperonin GroEL; Provisional |
1-531 |
0e+00 |
|
chaperonin GroEL; Provisional
Pssm-ID: 172594 Cd Length: 546 Bit Score: 787.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 1 MAAKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
Cdd:PRK14104 1 MSAKEVKFGVDARDRMLRGVDILANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 81 TNDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGL 160
Cdd:PRK14104 81 SADAAGDGTTTATVLAQAIVREGAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 161 DIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAV 240
Cdd:PRK14104 161 FLADAMKKVGNEGVITVEEAKSLETELDVVEGMQFDRGYISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 241 VQTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRA 320
Cdd:PRK14104 241 VQTGKPLVIVAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLQMLGRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 321 KKVSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDAL 400
Cdd:PRK14104 321 KKVMIDKENTTIVNGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 401 NATRAAVQEGIVPGGGVALLRSSVKIT-VKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYN 479
Cdd:PRK14104 401 HATRAAVEEGIVPGGGVALLRASEQLKgIKTKNDDQKTGVEIVRKALSAPARQIAINAGEDGSVIVGKILEKEQYSYGFD 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499269991 480 AQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 531
Cdd:PRK14104 481 SQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAG 532
|
|
| GroEL |
COG0459 |
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ... |
2-531 |
0e+00 |
|
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440227 Cd Length: 497 Bit Score: 781.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 2 AAKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKT 81
Cdd:COG0459 1 MAKQILFGEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPFENMGAQLVKEVASKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 82 NDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGLD 161
Cdd:COG0459 81 NDEAGDGTTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVDDKEELAQVATISANGDEEIGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 162 IAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAVV 241
Cdd:COG0459 161 IAEAMEKVGKDGVITVEEGKGLETELEVVEGMQFDKGYLSPYFVTDPEKMPAELENAYILLTDKKISSIQDLLPLLEKVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 242 QTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRAK 321
Cdd:COG0459 241 QSGKPLLIIAEDIDGEALATLVVNGIRGVLRVVAVKAPGFGDRRKAMLEDIAILTGGRVISEDLGLKLEDVTLDDLGRAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 322 KVSITKENTTIVDGAGQKSDIegrvaqikaqieettsdydreklqerlaklaggvaVIRVGGATEVEVKEKKDRIDDALN 401
Cdd:COG0459 321 RVEVDKDNTTIVEGAGNPKAI-----------------------------------VILVGAATEVEVKERKRRVEDALH 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 402 ATRAAVQEGIVPGGGVALLRSSVKI---TVKGENDDQdAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGY 478
Cdd:COG0459 366 ATRAAVEEGIVPGGGAALLRAARALrelAAKLEGDEQ-LGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAAKDKGFGF 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499269991 479 NAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPA 531
Cdd:COG0459 445 DAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
|
|
| groEL |
CHL00093 |
chaperonin GroEL |
3-528 |
0e+00 |
|
chaperonin GroEL
Pssm-ID: 177025 Cd Length: 529 Bit Score: 659.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 3 AKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKTN 82
Cdd:CHL00093 2 SKKILYQDNARRALERGMDILAEAVSVTLGPKGRNVVLEKKYGSPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 83 DIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGLDI 162
Cdd:CHL00093 82 DVAGDGTTTATVLAYAIVKQGMKNVAAGANPISLKRGIEKATQYVVSQIAEYARPVEDIQAITQVASISAGNDEEVGSMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 163 AEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNL-QAMLPVLEAVV 241
Cdd:CHL00093 162 ADAIEKVGREGVISLEEGKSTVTELEITEGMRFEKGFISPYFVTDTERMEVVQENPYILLTDKKITLVqQDLLPILEQVT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 242 QTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRAK 321
Cdd:CHL00093 242 KTKRPLLIIAEDVEKEALATLVLNKLRGIVNVVAVRAPGFGDRRKAMLEDIAILTGGQVITEDAGLSLETIQLDLLGQAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 322 KVSITKENTTIVdGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDALN 401
Cdd:CHL00093 322 RIIVTKDSTTII-ADGNEEQVKARCEQLRKQIEIADSSYEKEKLQERLAKLSGGVAVIKVGAATETEMKDKKLRLEDAIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 402 ATRAAVQEGIVPGGGVAL------LRSSVKITVKgenDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTdD 475
Cdd:CHL00093 401 ATKAAVEEGIVPGGGATLvhlsenLKTWAKNNLK---EDELIGALIVARAILAPLKRIAENAGKNGSVIIEKVQEQDF-E 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499269991 476 FGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKD 528
Cdd:CHL00093 477 IGYNAANNKFVNMYEAGIIDPAKVTRSALQNAASIASMILTTECIIVDKKESS 529
|
|
| PLN03167 |
PLN03167 |
Chaperonin-60 beta subunit; Provisional |
2-529 |
0e+00 |
|
Chaperonin-60 beta subunit; Provisional
Pssm-ID: 215611 [Multi-domain] Cd Length: 600 Bit Score: 556.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 2 AAKEVKFGR--SAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVAS 79
Cdd:PLN03167 55 AAKELHFNKdgSAIKKLQAGVNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPVENIGAKLVRQAAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 80 KTNDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSdEVAQVGTISANGEKQIG 159
Cdd:PLN03167 135 KTNDLAGDGTTTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVEDS-ELADVAAVSAGNNYEVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 160 LDIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEA 239
Cdd:PLN03167 214 NMIAEAMSKVGRKGVVTLEEGKSAENNLYVVEGMQFDRGYISPYFVTDSEKMSVEYDNCKLLLVDKKITNARDLIGILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 240 VVQTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGR 319
Cdd:PLN03167 294 AIRGGYPLLIIAEDIEQEALATLVVNKLRGSLKIAALKAPGFGERKSQYLDDIAILTGGTVIREEVGLSLDKVGKEVLGT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 320 AKKVSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDA 399
Cdd:PLN03167 374 AAKVVLTKDTTTIVGDGSTQEAVNKRVAQIKNLIEAAEQDYEKEKLNERIAKLSGGVAVIQVGAQTETELKEKKLRVEDA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 400 LNATRAAVQEGIVPGGGVALLRSSVK---ITVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDF 476
Cdd:PLN03167 454 LNATKAAVEEGIVVGGGCTLLRLASKvdaIKDTLENDEQKVGADIVKRALSYPLKLIAKNAGVNGSVVSEKVLSNDNPKF 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499269991 477 GYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDA 529
Cdd:PLN03167 534 GYNAATGKYEDLMAAGIIDPTKVVRCCLEHAASVAKTFLTSDCVVVEIKEPEP 586
|
|
| chaperonin_type_I_II |
cd00309 |
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ... |
4-522 |
1.24e-154 |
|
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 238189 Cd Length: 464 Bit Score: 449.96 E-value: 1.24e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 4 KEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTND 83
Cdd:cd00309 1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVE----HPAAKLLVEVAKSQDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 84 IAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDL--LAKAKKINTSDEVAQVGTISAN------GE 155
Cdd:cd00309 77 EVGDGTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILkeIAVPIDVEDREELLKVATTSLNsklvsgGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 156 KQIGLDIAEAMQKVG------NEGVITVEEAKT-AETELEVVEGMQFDRGYLSPYfvtnpekMVADLEDAFILLHEKKLS 228
Cdd:cd00309 157 DFLGELVVDAVLKVGkengdvDLGVIRVEKKKGgSLEDSELVVGMVFDKGYLSPY-------MPKRLENAKILLLDCKLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 229 NlqamlpvleavvqtgkplLIIAED-VEGEALATLVVnklrggLKIAAVKApgfgdRRKAMLEDIAILTGGTVISEdlgi 307
Cdd:cd00309 230 Y------------------VVIAEKgIDDEALHYLAK------LGIMAVRR-----VRKEDLERIAKATGATIVSR---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 308 kLESVTLDMLGRAKKVSITK----ENTTIVDGAGqksdiegrvaqikaqieettsdydreklqerlaklaGGVAVIRVGG 383
Cdd:cd00309 277 -LEDLTPEDLGTAGLVEETKigdeKYTFIEGCKG------------------------------------GKVATILLRG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 384 ATEVEVKEKKDRIDDALNATRAAVQE-GIVPGGGVALLRSSVKIT--VKGENDDQDAGVNIVRRALQSPARQIVENAGDE 460
Cdd:cd00309 320 ATEVELDEAERSLHDALCAVRAAVEDgGIVPGGGAAEIELSKALEelAKTLPGKEQLGIEAFADALEVIPRTLAENAGLD 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499269991 461 ASIVVGKILEKNTDDFGY---NAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIA 522
Cdd:cd00309 400 PIEVVTKLRAKHAEGGGNaggDVETGEIVDMKEAGIIDPLKVKRQALKSATEAASLILTIDDIIV 464
|
|
| Cpn60_TCP1 |
pfam00118 |
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ... |
23-521 |
7.70e-86 |
|
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
Pssm-ID: 395068 [Multi-domain] Cd Length: 489 Bit Score: 274.08 E-value: 7.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:pfam00118 1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHP----AAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 103 GAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAK---KINTSDEVAQVGTISANGeKQIGLD-------IAEAMQ----- 167
Cdd:pfam00118 77 AEKLLAAGVHPTTIIEGYEKALEKALEILDSIISipvEDVDREDLLKVARTSLSS-KIISREsdflaklVVDAVLaipkn 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 168 ----KVGNEGVITVEEAKTAETELevVEGMQFDRGYLSPyfvtnpeKMVADLEDAFILLHEKKLSN-------------- 229
Cdd:pfam00118 156 dgsfDLGNIGVVKILGGSLEDSEL--VDGVVLDKGPLHP-------DMPKRLENAKVLLLNCSLEYektetkatvvlsda 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 230 ----------LQAMLPVLEAVVQTGKPLLIIAEDVEGEALATLVVNKLRGGLKIaavkapgfgdrRKAMLEDIAILTGGT 299
Cdd:pfam00118 227 eqlerflkaeEEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRV-----------KKRDLERLAKATGAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 300 VISedlgiKLESVTLDMLGRAKKV---SITKENTTIVDGagqksdiegrvaqikaqieettsdydreklqerlaKLAGGV 376
Cdd:pfam00118 296 AVS-----SLDDLTPDDLGTAGKVeeeKIGDEKYTFIEG-----------------------------------CKSPKA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 377 AVIRVGGATEVEVKEKKDRIDDALNATRAAVQE-GIVPGGGVALLRSSVKI--TVKGENDDQDAGVNIVRRALQSPARQI 453
Cdd:pfam00118 336 ATILLRGATDHVLDEIERSIHDALCVVKNAIEDpRVVPGGGAVEMELARALreYAKSVSGKEQLAIEAFAEALEVIPKTL 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499269991 454 VENAGDEASIVVGKIL---EKNTDDFGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMI 521
Cdd:pfam00118 416 AENAGLDPIEVLAELRaahASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATEAASTILRIDDII 486
|
|
| chaperonin_like |
cd03333 |
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ... |
142-409 |
4.71e-41 |
|
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.
Pssm-ID: 239449 [Multi-domain] Cd Length: 209 Bit Score: 147.23 E-value: 4.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 142 DEVAQVGTISANGEKQIGLD-----IAEAMQKVG------NEGVITVEEAKTAE-TELEVVEGMQFDRGYLSPYfvtnpe 209
Cdd:cd03333 2 ELLLQVATTSLNSKLSSWDDflgklVVDAVLKVGpdnrmdDLGVIKVEKIPGGSlEDSELVVGVVFDKGYASPY------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 210 kMVADLEDAFILLHEKKLSNLqamlpvleavvqtgkpllIIAED-VEGEALATLVVnklrggLKIAAVKApgfgdRRKAM 288
Cdd:cd03333 76 -MPKRLENAKILLLDCPLEYV------------------VIAEKgIDDLALHYLAK------AGIMAVRR-----VKKED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 289 LEDIAILTGGTVISEdlgikLESVTLDMLGRAKKVSITK----ENTTIVDGAGqksdiegrvaqikaqieettsdydrek 364
Cdd:cd03333 126 LERIARATGATIVSS-----LEDLTPEDLGTAELVEETKigeeKLTFIEGCKG--------------------------- 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499269991 365 lqerlaklaGGVAVIRVGGATEVEVKEKKDRIDDALNATRAAVQE 409
Cdd:cd03333 174 ---------GKAATILLRGATEVELDEVKRSLHDALCAVRAAVEE 209
|
|
| cpn60 |
cd03343 |
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ... |
9-522 |
8.18e-22 |
|
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
Pssm-ID: 239459 [Multi-domain] Cd Length: 517 Bit Score: 98.87 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 9 GRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDIAGDG 88
Cdd:cd03343 13 GRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDI----EHPAAKMLVEVAKTQDEEVGDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 89 TTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDE-----VAQVGTISANGEKQIGL--D 161
Cdd:cd03343 89 TTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKdtlrkIAKTSLTGKGAEAAKDKlaD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 162 IA-EAMQKV--GNEGVITVE------EAKTAET--ELEVVEGMQFDRGYLS---PYFVTNPEKMVAD--LE--------- 216
Cdd:cd03343 169 LVvDAVLQVaeKRDGKYVVDldnikiEKKTGGSvdDTELIRGIVIDKEVVHpgmPKRVENAKIALLDapLEvkkteidak 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 217 ---------DAFIllhEKKLSNLQAMlpvLEAVVQTGKPLLIIAEDVEGEALATLVVNklrgglKIAAVKapgfgDRRKA 287
Cdd:cd03343 249 iritspdqlQAFL---EQEEAMLKEM---VDKIADTGANVVFCQKGIDDLAQHYLAKA------GILAVR-----RVKKS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 288 MLEDIAILTGGTVISedlgiKLESVTLDMLGRAKKVSITKenttivDGAGQKSDIEGrvaqikaqieettsdydreklqe 367
Cdd:cd03343 312 DMEKLARATGAKIVT-----NIDDLTPEDLGEAELVEERK------VGDDKMVFVEG----------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 368 rlAKLAGGVAVIrVGGATEVEVKEKKDRIDDALNATRAAVQEG-IVPGGGVALLRSSVKI-----TVKGEndDQDAgVNI 441
Cdd:cd03343 358 --CKNPKAVTIL-LRGGTEHVVDELERALEDALRVVADALEDGkVVAGGGAVEIELAKRLreyarSVGGR--EQLA-VEA 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 442 VRRALQSPARQIVENAGDEASIVVGKILEKNTDD---FGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTE 518
Cdd:cd03343 432 FADALEEIPRTLAENAGLDPIDTLVELRAAHEKGnknAGLDVYTGEVVDMLEKGVIEPLRVKKQAIKSATEAATMILRID 511
|
....
gi 499269991 519 AMIA 522
Cdd:cd03343 512 DVIA 515
|
|
| TCP1_zeta |
cd03342 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ... |
23-522 |
1.25e-13 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239458 [Multi-domain] Cd Length: 484 Bit Score: 73.06 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 23 LADAVKVTLGPKGR-NVVIDKSfGAPRITKDGVTVAKEIEledkFENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVR 101
Cdd:cd03342 24 LQDVLKTNLGPKGTlKMLVSGA-GDIKLTKDGNVLLSEMQ----IQHPTASMIARAATAQDDITGDGTTSNVLLIGELLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 102 EGAKAVAAGMNPMDLKRGIDLAVAEVVKDL--LAKAKKINTSDEVA-QVGTISANGEKQIGLdiAEAMQKVGNEGVITVE 178
Cdd:cd03342 99 QAERYIQEGVHPRIITEGFELAKNKALKFLesFKVPVEIDTDRELLlSVARTSLRTKLHADL--ADQLTEIVVDAVLAIY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 179 EAkTAETELEVVEGMQFD----------RGYLSPYFVTNPEkMVADLEDAFILL------HEKKLSNLQamlpVLEAVVQ 242
Cdd:cd03342 177 KP-DEPIDLHMVEIMQMQhksdsdtkliRGLVLDHGARHPD-MPKRVENAYILTcnvsleYEKTEVNSG----FFYSVVI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 243 TGKPLLIIAEDVEGEAlatlvvnklrgglKIAAVkapgfgdrRKAM---LEDIAILTGGTVISEdlgikLESVTLDMLGR 319
Cdd:cd03342 251 NQKGIDPPSLDMLAKE-------------GILAL--------RRAKrrnMERLTLACGGVAMNS-----VDDLSPECLGY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 320 AKKV---SITKENTTIvdgagqksdiegrvaqikaqIEETTsdydreklqerlaklAGGVAVIRVGGATEVEVKEKKDRI 396
Cdd:cd03342 305 AGLVyerTLGEEKYTF--------------------IEGVK---------------NPKSCTILIKGPNDHTITQIKDAI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 397 DDALNATRAAVQEG-IVPGGG---VAL---LRSSVKiTVKGENddqDAGVNIVRRALQSPARQIVENAGDEASIVVGKIL 469
Cdd:cd03342 350 RDGLRAVKNAIEDKcVVPGAGafeVALyahLKEFKK-SVKGKA---KLGVQAFADALLVIPKTLAENSGLDVQETLVKLQ 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 499269991 470 EKNTDD---FGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVAS-LLITTEAMIA 522
Cdd:cd03342 426 DEYAEGgqvGGVDLDTGEPMDPESEGIWDNYSVKRQILHSATVIASqLLLVDEIIRA 482
|
|
| TCP1_beta |
cd03336 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ... |
3-145 |
6.47e-13 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239452 [Multi-domain] Cd Length: 517 Bit Score: 71.21 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 3 AKEVKfGRSAREKMLRGVDILADAVKVTLGPKGRNVVI--DKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASK 80
Cdd:cd03336 6 AQEEK-GETARLSSFVGAIAIGDLVKTTLGPKGMDKILqsVGRSGGVTVTNDGATILKSIGVD----NPAAKVLVDISKV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499269991 81 TNDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKiNTSDEVA 145
Cdd:cd03336 81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVD-HSSDEEA 144
|
|
| chap_CCT_zeta |
TIGR02347 |
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ... |
23-522 |
8.48e-13 |
|
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274088 [Multi-domain] Cd Length: 531 Bit Score: 70.53 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:TIGR02347 28 LQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQ----HPTASMIARAATAQDDITGDGTTSTVLLIGELLKQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 103 GAKAVAAGMNPMDLKRGIDLAVAEVVKDLLA-KAKKINTSDEVAQVGTISANGEKQIGLDIAEAMQKVGNEGVITVEEAK 181
Cdd:TIGR02347 104 AERYILEGVHPRIITEGFEIARKEALQFLDKfKVKKEDEVDREFLLNVARTSLRTKLPADLADQLTEIVVDAVLAIKKDG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 182 TA---------------ETELEVVEGMQFDRGYLSPyfvtnpeKMVADLEDAFILLHEKKLsnlqamlpvleavvqtgkp 246
Cdd:TIGR02347 184 EDidlfmveimemkhksATDTTLIRGLVLDHGARHP-------DMPRRVKNAYILTCNVSL------------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 247 lliiaEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTG-----GTVISEDLGIKLESvtLDMLGRAK 321
Cdd:TIGR02347 238 -----EYEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKKKVCGkspdkGFVVINQKGIDPPS--LDLLAKEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 322 KVSITK------ENTTIVDGAGQKSDIEGRVAQI---KAQIEETTSDYDREKLQERLAKLAGGVAVIRvgGATEVEVKEK 392
Cdd:TIGR02347 311 IMALRRakrrnmERLTLACGGEALNSVEDLTPEClgwAGLVYETTIGEEKYTFIEECKNPKSCTILIK--GPNDHTIAQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 393 KDRIDDALNATRAAVQEG-IVPGGG---VALLRS--SVKITVKGEnddQDAGVNIVRRALQSPARQIVENAGDEASIVVG 466
Cdd:TIGR02347 389 KDAVRDGLRAVKNAIEDKcVVPGAGafeIAAYRHlkEYKKSVKGK---AKLGVEAFANALLVIPKTLAENSGFDAQDTLV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 467 KILEKNTDDF---GYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVAS-LLITTEAMIA 522
Cdd:TIGR02347 466 KLEDEHDEGGevvGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASqLLLVDEVMRA 525
|
|
| TCP1_delta |
cd03338 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ... |
23-514 |
2.44e-12 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239454 [Multi-domain] Cd Length: 515 Bit Score: 69.24 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMvrevaSKTNDI-AGDGTTTATVLAQAIVR 101
Cdd:cd03338 20 VADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVEL-----SKAQDIeAGDGTTSVVVLAGALLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 102 EGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVA--QVGTISANGE------KQIGLDIAEAMQKVGNEG 173
Cdd:cd03338 95 ACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESliKSATTSLNSKvvsqysSLLAPIAVDAVLKVIDPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 174 VITVEEAK----------TAETElEVVEGMQFD-RGYLSPYFVTNPEKMV------------ADLEDAFI---------L 221
Cdd:cd03338 175 TATNVDLKdirivkklggTIEDT-ELVDGLVFTqKASKKAGGPTRIEKAKigliqfclsppkTDMDNNIVvndyaqmdrI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 222 LHEKKlsnlQAMLPVLEAVVQTGKPLLIIAEDVEGEALATLVVNKLRgGLKIAAVKAPgfgDRrkamlEDIAIltggtvI 301
Cdd:cd03338 254 LREER----KYILNMCKKIKKSGCNVLLIQKSILRDAVSDLALHFLA-KLKIMVVKDI---ER-----EEIEF------I 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 302 SEDLGIK----LESVTLDMLGRAKKVsitkenttivdgagqksdiegrvaqikaqiEETTSDYDREKLQERLAKLAGGVA 377
Cdd:cd03338 315 CKTIGCKpvasIDHFTEDKLGSADLV------------------------------EEVSLGDGKIVKITGVKNPGKTVT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 378 VIrVGGATEVEVKEKKDRIDDALNATRAAVQE-GIVPGGGVALLRSSVKITvkgENDDQDAGVNIV-----RRALQSPAR 451
Cdd:cd03338 365 IL-VRGSNKLVLDEAERSLHDALCVIRCLVKKrALIPGGGAPEIEIALQLS---EWARTLTGVEQYcvrafADALEVIPY 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499269991 452 QIVENAGDEASIVVGKILEKNTD---DFGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAA-SVASLL 514
Cdd:cd03338 441 TLAENAGLNPISIVTELRNRHAQgekNAGINVRKGAITNILEENVVQPLLVSTSAITLATeTVRMIL 507
|
|
| PTZ00212 |
PTZ00212 |
T-complex protein 1 subunit beta; Provisional |
3-145 |
1.18e-11 |
|
T-complex protein 1 subunit beta; Provisional
Pssm-ID: 185514 Cd Length: 533 Bit Score: 66.98 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 3 AKEVKfGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPR-----ITKDGVTVAKEIELEdkfeNMGAQMVREV 77
Cdd:PTZ00212 15 AQEEK-GETARLQSFVGAIAVADLVKTTLGPKGMDKILQPMSEGPRsgnvtVTNDGATILKSVWLD----NPAAKILVDI 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499269991 78 ASKTNDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVaEVVKDLLAKAKKINTSDEVA 145
Cdd:PTZ00212 90 SKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMAL-DVARKALEEIAFDHGSDEEK 156
|
|
| chap_CCT_beta |
TIGR02341 |
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ... |
9-527 |
2.90e-10 |
|
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274082 Cd Length: 519 Bit Score: 62.57 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 9 GRSAREKMLRGVDILADAVKVTLGPKGRNVVI--DKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDIAG 86
Cdd:TIGR02341 12 AENARLSSFVGAIAIGDLVKSTLGPKGMDKILqsSSSDASIMVTNDGATILKSIGVD----NPAAKVLVDMSKVQDDEVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 87 DGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAeVVKDLLAKAKKINTSDEV---------------AQVGTIS 151
Cdd:TIGR02341 88 DGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATK-AARDALLKSAVDNGSDEVkfrqdlmniarttlsSKILSQH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 152 ANGEKQIGLDIAEAMQKVGNEGVITVEE---AKTAETELEvvEGMQFDR--GYLSPYFVTNPEKMVADL---EDAFILLH 223
Cdd:TIGR02341 167 KDHFAQLAVDAVLRLKGSGNLEAIQIIKklgGSLADSYLD--EGFLLDKkiGVNQPKRIENAKILIANTgmdTDKVKIFG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 224 EKKLSNLQAMLPVLEAVVQ---TGKPLLIIAEDVEGEALATLVVN---KLRGGLKIAAVKAPGFGDrrkamLEDIAILTG 297
Cdd:TIGR02341 245 SRVRVDSTAKVAELEHAEKekmKEKVEKILKHGINCFINRQLIYNypeQLFADAGVMAIEHADFEG-----VERLALVTG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 298 GTVISedlgiKLESVTLDMLGRAKKvsitkenttivdgagqksdiegrvaqikaqIEETTSDYDreKLQERLAKLAGGVA 377
Cdd:TIGR02341 320 GEIVS-----TFDHPELVKLGSCDL------------------------------IEEIMIGED--KLLKFSGVKLGEAC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 378 VIRVGGATEVEVKEKKDRIDDALNATRAAVQEG-IVPGGGVALLRSSVKITVKGENDD--QDAGVNIVRRALQSPARQIV 454
Cdd:TIGR02341 363 TIVLRGATQQILDEAERSLHDALCVLSQTVKESrTVLGGGCSEMLMSKAVTQEAQRTPgkEALAVEAFARALRQLPTIIA 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499269991 455 ENAGDEASIVVGKILEKNTD---DFGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKK 527
Cdd:TIGR02341 443 DNAGFDSAELVAQLRAAHYNgntTMGLDMNEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNIIKAAPRK 518
|
|
| chap_CCT_delta |
TIGR02342 |
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ... |
8-142 |
3.60e-10 |
|
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274083 Cd Length: 517 Bit Score: 62.49 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 8 FGRSAREKMLRGVDILA-----DAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVaSKTN 82
Cdd:TIGR02342 1 FQDKDKPQDVRTSNIVAakavaDAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVL----HPAAKMLVEL-SKAQ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499269991 83 DI-AGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSD 142
Cdd:TIGR02342 76 DIeAGDGTTSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSD 136
|
|
| chap_CCT_eta |
TIGR02345 |
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ... |
23-521 |
7.96e-10 |
|
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274086 [Multi-domain] Cd Length: 523 Bit Score: 61.31 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:TIGR02345 30 IAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDI----VHPAAKTLVDIAKSQDAEVGDGTTSVTILAGELLKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 103 GAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSD----EVAQVGTISANGEKQIG----------------LDI 162
Cdd:TIGR02345 106 AKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqrELLEKCAATALSSKLIShnkeffskmivdavlsLDR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 163 AEAMQKVgnEGVITVEEAKTAETELevVEGMQFDRGYLSPYFVTNPEK----MVADLEDAFILLHEK-----KLSNLQAM 233
Cdd:TIGR02345 186 DDLDLKL--IGIKKVQGGALEDSQL--VNGVAFKKTFSYAGFEQQPKKfanpKILLLNVELELKAEKdnaeiRVEDVEDY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 234 LPVLEAVVQtgkpllIIAEDVEG--EALATLVVNKlrggLKIAAVKAPGFGDRRkamlediaILTGGTVISEDlgikles 311
Cdd:TIGR02345 262 QAIVDAEWA------IIFRKLEKivESGANVVLSK----LPIGDLATQYFADRD--------IFCAGRVSAED------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 312 vtldmLGRAKKVSITKENTTIvdgagqkSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRvGGATEVeVKE 391
Cdd:TIGR02345 317 -----LKRVIKACGGSIQSTT-------SDLEADVLGTCALFEERQIGSERYNYFTGCPHAKTCTIILR-GGAEQF-IEE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 392 KKDRIDDALNATRAAVQ-EGIVPGGGV------ALLRSSVKITvkgeNDDQDAGVNIVRRALQSPARQIVENAGDEASIV 464
Cdd:TIGR02345 383 AERSLHDAIMIVRRALKnKKIVAGGGAiemelsKCLRDYSKTI----DGKQQLIINAFAKALEIIPRQLCENAGFDSIEI 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 465 VGKILEKNTDD---FGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMI 521
Cdd:TIGR02345 459 LNKLRSRHAKGgkwYGVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
|
|
| chap_CCT_alpha |
TIGR02340 |
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ... |
9-176 |
2.71e-09 |
|
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274081 [Multi-domain] Cd Length: 536 Bit Score: 59.73 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 9 GRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVREVASKTNDIAGDG 88
Cdd:TIGR02340 10 GQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDREVGDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 89 TTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVK----------DLLAKAKKINTSDEVAQVGTISANGE--K 156
Cdd:TIGR02340 86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKyikenlsvsvDELGREALINVAKTSMSSKIIGLDSDffS 165
|
170 180
....*....|....*....|
gi 499269991 157 QIGLDIAEAMQKVGNEGVIT 176
Cdd:TIGR02340 166 NIVVDAVLAVKTTNENGETK 185
|
|
| TCP1_theta |
cd03341 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ... |
23-521 |
8.82e-09 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239457 [Multi-domain] Cd Length: 472 Bit Score: 58.00 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 23 LADAVKVTLGPKGRN--VV--IDKSFgaprITKDGVTVAKEIEledkFENMGAQMVREvASKTNDI-AGDGTTTATVLAQ 97
Cdd:cd03341 20 LSQITRTSYGPNGMNkmVInhLEKLF----VTSDAATILRELE----VQHPAAKLLVM-ASQMQEEeIGDGTNLVVVLAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 98 AIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDL----LAKAKKINTSDEVAQVgTISANGEKQIGLD------IAEAMQ 167
Cdd:cd03341 91 ELLEKAEELLRMGLHPSEIIEGYEKALKKALEILeelvVYKIEDLRNKEEVSKA-LKTAIASKQYGNEdflsplVAEACI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 168 KV--GNEGVITVEEAKTAE------TELEVVEGMQFDRgylspyfvtNPEKMVADLEDAFILlhekklsnlqamlpVLEA 239
Cdd:cd03341 170 SVlpENIGNFNVDNIRVVKilggslEDSKVVRGMVFKR---------EPEGSVKRVKKAKVA--------------VFSC 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 240 VVQTGKPLLIIAEDVEGEALATLvvNKlrggLKIAAVKAPG-FGDRRkamledIAILTGGTVIsedlgIKLESVTLDMLG 318
Cdd:cd03341 227 PFDIGVNVIVAGGSVGDLALHYC--NK----YGIMVIKINSkFELRR------LCRTVGATPL-----PRLGAPTPEEIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 319 RAKKVSITkenttivdgagqksDIEGRVAQIKAQIEETTSdydreklqerlaklaggVAVIRVGGATEVEVKEKKDRIDD 398
Cdd:cd03341 290 YCDSVYVE--------------EIGDTKVVVFRQNKEDSK-----------------IATIVLRGATQNILDDVERAIDD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 399 ALNATRAAVQEG-IVPGGGVALLRSSVKITVKGEND---DQDAgVNIVRRALQSPARQIVENAGDEASIVVGKIL---EK 471
Cdd:cd03341 339 GVNVFKSLTKDGrFVPGAGATEIELAKKLKEYGEKTpglEQYA-IKKFAEAFEVVPRTLAENAGLDATEVLSELYaahQK 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499269991 472 NTDDFGYNAQTGEYG--DMIAMGIIDPVKVVRTALQDAASVASLLITTEAMI 521
Cdd:cd03341 418 GNKSAGVDIESGDEGtkDAKEAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
|
|
| TCP1_eta |
cd03340 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ... |
22-131 |
1.02e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239456 [Multi-domain] Cd Length: 522 Bit Score: 54.60 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 22 ILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELedkfenmgaqmVREVASKTNDIA-------GDGTTTATV 94
Cdd:cd03340 27 AIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDI-----------VHPAAKTLVDIAksqdaevGDGTTSVVV 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 499269991 95 LAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDL 131
Cdd:cd03340 96 LAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKI 132
|
|
| chap_CCT_epsi |
TIGR02343 |
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ... |
13-522 |
3.18e-07 |
|
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274084 [Multi-domain] Cd Length: 532 Bit Score: 52.88 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 13 REKMLRGVDIL----------ADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKFENMgaqMVREVASKTN 82
Cdd:TIGR02343 19 NKKRLKGLEAKksniaaaksvASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKL---MVELSKSQDD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 83 DIaGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKIntSDEVAQVGTISANGEKQIGLDI 162
Cdd:TIGR02343 96 EI-GDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEI--SADNNNREPLIQAAKTSLGSKI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 163 A----EAMQKVGNEGVITVEEAKTAETELEVV----------EGMQFDRGYLSPYFVTNPEkMVADLEDAFILL------ 222
Cdd:TIGR02343 173 VskchRRFAEIAVDAVLNVADMERRDVDFDLIkvegkvggslEDTKLIKGIIIDKDFSHPQ-MPKEVEDAKIAIltcpfe 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 223 -------HEKKLSNL-----------QAMLPVLEAVVQTGKPLLIIAEDVEGEALATLVVNKLrgglkiAAVKAPGFGDr 284
Cdd:TIGR02343 252 ppkpktkHKLDISSVeeykklqkyeqQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDL------PAVRWVGGQE- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 285 rkamLEDIAILTGGTVISedlgiKLESVTLDMLGRAKKV-----SITKENTTIVDGAGQKSDIegrvaqikaqieettsd 359
Cdd:TIGR02343 325 ----LELIAIATGGRIVP-----RFQELSKDKLGKAGLVreisfGTTKDRMLVIEQCKNSKAV----------------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 360 ydreklqerlaklaggvaVIRVGGATEVEVKEKKDRIDDALNATRAAVQEG-IVPGGGVALLrsSVKITVKGEND----- 433
Cdd:TIGR02343 379 ------------------TIFIRGGNKMIIEEAKRSIHDALCVVRNLIKDSrIVYGGGAAEI--SCSLAVSQEADkypgv 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 434 DQDAgVNIVRRALQSPARQIVENAG----DEASIVVGKILEKNTDDFGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAAS 509
Cdd:TIGR02343 439 EQYA-IRAFADALETIPMALAENSGldpiGTLSTLKSLQLKEKNPNLGVDCLGYGTNDMKEQFVFETLIGKKQQILLATQ 517
|
570
....*....|...
gi 499269991 510 VASLLITTEAMIA 522
Cdd:TIGR02343 518 LVRMILKIDDVIS 530
|
|
| TCP1_alpha |
cd03335 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ... |
9-129 |
5.22e-07 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239451 Cd Length: 527 Bit Score: 52.29 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 9 GRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVREVASKTNDIAGDG 88
Cdd:cd03335 6 GQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHP----AAKILVELAQLQDKEVGDG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 499269991 89 TTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVK 129
Cdd:cd03335 82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVK 122
|
|
| TCP1_epsilon |
cd03339 |
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ... |
12-143 |
4.07e-06 |
|
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
Pssm-ID: 239455 Cd Length: 526 Bit Score: 49.60 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 12 AREKMLRGVD-----IL-----ADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKT 81
Cdd:cd03339 14 EKKKRLKGLEahkshILaaksvANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVD----HQIAKLLVELSKSQ 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499269991 82 NDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDE 143
Cdd:cd03339 90 DDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADKIEFSPD 151
|
|
| chap_CCT_theta |
TIGR02346 |
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ... |
23-159 |
6.77e-04 |
|
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274087 [Multi-domain] Cd Length: 531 Bit Score: 42.40 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 23 LADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDIAGDGTTTATVLAQAIVRE 102
Cdd:TIGR02346 30 LSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQ----HPAAKLLVMASEMQENEIGDGTNLVLVLAGELLNK 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499269991 103 GAKAVAAGMNPMDLKRGIDLAVAEVVKDL----LAKAKKINTSDEVAQVgTISANGEKQIG 159
Cdd:TIGR02346 106 AEELIRMGLHPSEIIKGYEMALKKAMEILeelvVWEVKDLRDKDELIKA-LKASISSKQYG 165
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
9-152 |
1.78e-03 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 40.88 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 9 GRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVTVAKEIELEdkfeNMGAQMVREVASKTNDIAGDG 88
Cdd:TIGR02344 14 GRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVA----HPAAKSMIELSRTQDEEVGDG 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499269991 89 TTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISA 152
Cdd:TIGR02344 90 TTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQS 153
|
|
| chap_CCT_gamma |
TIGR02344 |
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ... |
383-527 |
9.17e-03 |
|
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
Pssm-ID: 274085 [Multi-domain] Cd Length: 524 Bit Score: 38.57 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269991 383 GATEVEVKEKKDRIDDALNATRAAVQEG-IVPGGGVALLRSSVKITVKGE--NDDQDAGVNIVRRALQSPARQIVENAGD 459
Cdd:TIGR02344 373 GASKDILNEVERNLQDAMAVARNVLLDPkLVPGGGATEMAVSVALTEKSKklEGVEQWPYRAVADALEIIPRTLAQNCGA 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499269991 460 EASIVVGKILEKNTDD----FGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKK 527
Cdd:TIGR02344 453 NVIRTLTELRAKHAQEnnctWGIDGETGKIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
|
|
| |
